ID   XYNA_ASPKW              Reviewed;         327 AA.
AC   P33559; G7Y054;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xynA; ORFNames=AKAW_10666;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-33; 41-54; 63-76
RP   AND 76-100, AND PYROGLUTAMATE FORMATION AT GLN-26.
RC   STRAIN=NBRC 4308;
RX   PubMed=1368254; DOI=10.1271/bbb.56.906;
RA   Ito K., Ikemasu T., Ishikawa T.;
RT   "Cloning and sequencing of the xynA gene encoding xylanase A of Aspergillus
RT   kawachii.";
RL   Biosci. Biotechnol. Biochem. 56:906-912(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=GAA92552.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; D14847; BAA03575.1; -; Genomic_DNA.
DR   EMBL; DF126496; GAA92552.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P33559; -.
DR   SMR; P33559; -.
DR   STRING; 1033177.P33559; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   eggNOG; ENOG502QSCW; Eukaryota.
DR   InParanoid; P33559; -.
DR   OrthoDB; 9074at5052; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.20.20.80:FF:000094; Endo-1,4-beta-xylanase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:1368254"
FT   CHAIN           26..327
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007965"
FT   DOMAIN          55..326
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   MOD_RES         26
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1368254"
FT   DISULFID        281..287
FT                   /evidence="ECO:0000250"
FT   CONFLICT        33
FT                   /note="T -> S (in Ref. 1; BAA03575/AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="I -> V (in Ref. 1; BAA03575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="E -> D (in Ref. 1; BAA03575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  35480 MW;  93B3D04F22F5D4FF CRC64;
     MVQIKAAALA MLFASHVLSE PIEPRQASVS IDTKFKAHGK KYLGNIGDQY TLTKNSKTPA
     IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ SNNKLIRGHT LVWHSQLPSW
     VQAITDKNTL IEVMKNHITT VMQHYKGKIY AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR
     IAFETARAAD PNAKLYINDY NLDSASYPKL AGMVSHVKKW IEAGIPIDGI GSQTHLSAGG
     GAGISGALNA LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLDQPKCIGI TVWGVADPDS
     WRSSSTPLLF DSNYNPKPAY TAIANAL
//